MolNFT v1 · #38619 · protein

Crystal structure of the S554A/M564G mutant of murine carnitine acetyltransferase in complex with hexanoylcarnitine and CoA

2H3W: “Crystal structure of the S554A/M564G mutant of murine carnitine acetyltransferase in complex with…”. X-ray diffraction, 2 ligands (COA, HC5), 10 pockets (best druggability 0.78). MolNFT v1 #38619 on GenesisL1: 3D structure, binding…

PDB: 2H3W
Type: protein
Length: 1,198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carnitine acetyltransferase
UniProt: Q3V1Y3
Ligands: COA, HC5
Pockets: 10 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Carnitine acetyltransferase	protein	599	45% helix, 15% strand	Q3V1Y3

Ligands and binding sites

COA · Coenzyme A · ligand · 2 copies · chains A, B
HC5 · (R)-3-carboxy-2-(hexanoyloxy)-N,N,N-trimethylpropan-1-aminium · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	860	0.78	0.81	90	COA, HC5
2	865	0.77	0.80	83	COA, HC5
3	176	0.56	0.80	24	empty
4	174	0.54	0.80	28	empty
5	76	0.47	0.82	20	empty

Compared structures

2H3W · Crystal structure of the S554A/M564G mutant of murine carnitine acetyltransferase in… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q3V1Y3
Elsewhere: RCSB PDB 2H3W · PDBe 2H3W · UniProt Q3V1Y3

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